ID NB5R3_RAT Reviewed; 301 AA.
AC P20070; Q64569; Q64720;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 24-JAN-2024, entry version 202.
DE RecName: Full=NADH-cytochrome b5 reductase 3 {ECO:0000305};
DE Short=B5R;
DE Short=Cytochrome b5 reductase;
DE EC=1.6.2.2 {ECO:0000269|PubMed:11695905, ECO:0000269|PubMed:8812833, ECO:0000269|PubMed:8978818};
DE AltName: Full=Diaphorase-1 {ECO:0000250|UniProtKB:P00387};
GN Name=Cyb5r3 {ECO:0000312|RGD:2502}; Synonyms=Dia1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=2391344; DOI=10.1093/oxfordjournals.jbchem.a123130;
RA Zenno S., Hattori M., Misumi Y., Yubisui T., Sakaki Y.;
RT "Molecular cloning of a cDNA encoding rat NADH-cytochrome b5 reductase and
RT the corresponding gene.";
RL J. Biochem. 107:810-816(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=3174630; DOI=10.1073/pnas.85.19.7246;
RA Pietrini G., Carrera P., Borgese N.;
RT "Two transcripts encode rat cytochrome b5 reductase.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7246-7250(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-37 (ISOFORMS 2 AND 3), TISSUE SPECIFICITY,
RP ALTERNATIVE PROMOTER USAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley, and Wistar; TISSUE=Liver, and Reticulocyte;
RX PubMed=1577871; DOI=10.1083/jcb.117.5.975;
RA Pietrini G., Aggujaro D., Carrera P., Malyszko J., Vitale A., Borgese N.;
RT "A single mRNA, transcribed from an alternative, erythroid-specific,
RT promoter, codes for two non-myristylated forms of NADH-cytochrome b5
RT reductase.";
RL J. Cell Biol. 117:975-986(1992).
RN [5]
RP PROTEIN SEQUENCE OF 2-25, AND MYRISTOYLATION AT GLY-2.
RC TISSUE=Liver;
RX PubMed=2498303; DOI=10.1093/oxfordjournals.jbchem.a122659;
RA Murakami K., Yubisui T., Takeshita M., Miyata T.;
RT "The NH2-terminal structures of human and rat liver microsomal NADH-
RT cytochrome b5 reductases.";
RL J. Biochem. 105:312-317(1989).
RN [6]
RP PROTEIN SEQUENCE OF 33-43, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8812833; DOI=10.1006/prep.1996.0072;
RA Barber M.J., Quinn G.B.;
RT "High-level expression in Escherichia coli of the soluble, catalytic domain
RT of rat hepatic cytochrome b5 reductase.";
RL Protein Expr. Purif. 8:41-47(1996).
RN [7]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=8143727; DOI=10.1111/j.1432-1033.1994.tb18673.x;
RA Mota Vieira L., Kaplan J.-C., Kahn A., Leroux A.;
RT "Heterogeneity of the rat NADH-cytochrome-b5-reductase transcripts
RT resulting from multiple alternative first exons.";
RL Eur. J. Biochem. 220:729-737(1994).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY,
RP MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
RX PubMed=8978818; DOI=10.1083/jcb.135.6.1501;
RA Borgese N., Aggujaro D., Carrera P., Pietrini G., Bassetti M.;
RT "A role for N-myristoylation in protein targeting: NADH-cytochrome b5
RT reductase requires myristic acid for association with outer mitochondrial
RT but not ER membranes.";
RL J. Cell Biol. 135:1501-1513(1996).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 34-301 IN COMPLEX WITH FAD AND
RP NAD(+), FAD-BINDING, COFACTOR, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LYS-111.
RX PubMed=11695905; DOI=10.1021/bi0106336;
RA Bewley M.C., Marohnic C.C., Barber M.J.;
RT "The structure and biochemistry of NADH-dependent cytochrome b5 reductase
RT are now consistent.";
RL Biochemistry 40:13574-13582(2001).
CC -!- FUNCTION: Catalyzes the reduction of two molecules of cytochrome b5
CC using NADH as the electron donor. {ECO:0000269|PubMed:11695905,
CC ECO:0000269|PubMed:8812833, ECO:0000269|PubMed:8978818}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] +
CC H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2;
CC Evidence={ECO:0000269|PubMed:11695905, ECO:0000269|PubMed:8812833,
CC ECO:0000269|PubMed:8978818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46681;
CC Evidence={ECO:0000305|PubMed:11695905};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11695905, ECO:0000269|PubMed:8812833};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for 2 Fe(III)-[cytochrome b5] {ECO:0000269|PubMed:8812833};
CC KM=10 uM for 2 Fe(III)-[cytochrome b5] {ECO:0000269|PubMed:11695905};
CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC cytochrome b5 reductase (CYB5R3) and MTARC2 (By similarity). Interacts
CC with MTLN; the interaction is required to maintain cellular lipid
CC composition and leads to stimulation of mitochondrial respiratory
CC complex I activity (By similarity). {ECO:0000250|UniProtKB:P83686,
CC ECO:0000250|UniProtKB:Q9DCN2}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8978818}; Lipid-anchor
CC {ECO:0000269|PubMed:8978818}; Cytoplasmic side
CC {ECO:0000305|PubMed:8978818}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:8978818}; Lipid-anchor
CC {ECO:0000269|PubMed:8978818}; Cytoplasmic side
CC {ECO:0000305|PubMed:8978818}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:1577871}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative initiation; Named isoforms=3;
CC Name=1; Synonyms=L-form reticulocyte reductase;
CC IsoId=P20070-1; Sequence=Displayed;
CC Name=2; Synonyms=R-form reticulocyte reductase;
CC IsoId=P20070-2; Sequence=VSP_009661;
CC Name=3; Synonyms=Soluble form;
CC IsoId=P20070-3; Sequence=VSP_009660;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Ubiquitously expressed.
CC {ECO:0000269|PubMed:1577871, ECO:0000269|PubMed:8143727}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Ubiquitously expressed.
CC {ECO:0000269|PubMed:8143727}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed only in erythroid tissues,
CC reticulocytes and liver. {ECO:0000269|PubMed:1577871,
CC ECO:0000269|PubMed:8143727}.
CC -!- PTM: [Isoform 1]: Myristoylated. {ECO:0000269|PubMed:2498303,
CC ECO:0000269|PubMed:8978818}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; D00636; BAA00530.1; -; mRNA.
DR EMBL; J03867; AAA41008.1; -; mRNA.
DR EMBL; BC062066; AAH62066.1; -; mRNA.
DR EMBL; X65191; CAA46308.1; -; mRNA.
DR EMBL; X65191; CAA46309.1; -; mRNA.
DR EMBL; X65190; CAA46307.1; -; Genomic_DNA.
DR EMBL; X77117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A40495; RDRTB5.
DR PIR; S23641; S23641.
DR RefSeq; NP_620232.1; NM_138877.1. [P20070-1]
DR RefSeq; XP_006242127.1; XM_006242065.3. [P20070-2]
DR PDB; 1I7P; X-ray; 2.00 A; A=34-301.
DR PDB; 1IB0; X-ray; 2.30 A; A=34-301.
DR PDB; 1QX4; X-ray; 1.80 A; A/B=34-301.
DR PDBsum; 1I7P; -.
DR PDBsum; 1IB0; -.
DR PDBsum; 1QX4; -.
DR AlphaFoldDB; P20070; -.
DR SMR; P20070; -.
DR CORUM; P20070; -.
DR IntAct; P20070; 3.
DR STRING; 10116.ENSRNOP00000061381; -.
DR ChEMBL; CHEMBL4523194; -.
DR GlyGen; P20070; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P20070; -.
DR PhosphoSitePlus; P20070; -.
DR SwissPalm; P20070; -.
DR jPOST; P20070; -.
DR PaxDb; 10116-ENSRNOP00000012878; -.
DR Ensembl; ENSRNOT00000102247.1; ENSRNOP00000077900.1; ENSRNOG00000009592.7. [P20070-1]
DR Ensembl; ENSRNOT00000111302.1; ENSRNOP00000082175.1; ENSRNOG00000009592.7. [P20070-2]
DR Ensembl; ENSRNOT00055052922; ENSRNOP00055043732; ENSRNOG00055030420. [P20070-1]
DR Ensembl; ENSRNOT00060051599; ENSRNOP00060042911; ENSRNOG00060029632. [P20070-1]
DR Ensembl; ENSRNOT00065056564; ENSRNOP00065046543; ENSRNOG00065032895. [P20070-1]
DR GeneID; 25035; -.
DR KEGG; rno:25035; -.
DR AGR; RGD:2502; -.
DR CTD; 1727; -.
DR RGD; 2502; Cyb5r3.
DR eggNOG; KOG0534; Eukaryota.
DR GeneTree; ENSGT00940000153962; -.
DR HOGENOM; CLU_003827_9_2_1; -.
DR InParanoid; P20070; -.
DR OMA; KGPEMQK; -.
DR OrthoDB; 979728at2759; -.
DR PhylomeDB; P20070; -.
DR TreeFam; TF314333; -.
DR BRENDA; 1.6.2.2; 5301.
DR Reactome; R-RNO-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-RNO-211945; Phase I - Functionalization of compounds.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR SABIO-RK; P20070; -.
DR EvolutionaryTrace; P20070; -.
DR PRO; PR:P20070; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000009592; Expressed in lung and 19 other cell types or tissues.
DR Genevisible; P20070; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISO:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:1903958; C:nitric-oxide synthase complex; ISO:RGD.
DR GO; GO:0043531; F:ADP binding; IDA:RGD.
DR GO; GO:0016208; F:AMP binding; IDA:RGD.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
DR GO; GO:0051287; F:NAD binding; IDA:RGD.
DR GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:Ensembl.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; ISO:RGD.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1.
DR PANTHER; PTHR19370:SF121; NADH-CYTOCHROME B5 REDUCTASE 3; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation;
KW Alternative promoter usage; Cholesterol biosynthesis;
KW Cholesterol metabolism; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; FAD; Flavoprotein; Lipid biosynthesis;
KW Lipid metabolism; Lipoprotein; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Myristate; NAD; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2498303,
FT ECO:0000269|PubMed:8978818"
FT CHAIN 2..301
FT /note="NADH-cytochrome b5 reductase 3"
FT /id="PRO_0000019401"
FT DOMAIN 40..152
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 92
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11695905,
FT ECO:0007744|PDB:1I7P, ECO:0007744|PDB:1IB0"
FT BINDING 93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11695905,
FT ECO:0007744|PDB:1I7P, ECO:0007744|PDB:1IB0"
FT BINDING 94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11695905,
FT ECO:0007744|PDB:1I7P, ECO:0007744|PDB:1IB0"
FT BINDING 109
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11695905,
FT ECO:0007744|PDB:1I7P, ECO:0007744|PDB:1IB0"
FT BINDING 111
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11695905,
FT ECO:0007744|PDB:1I7P, ECO:0007744|PDB:1IB0"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11695905,
FT ECO:0007744|PDB:1I7P, ECO:0007744|PDB:1IB0"
FT BINDING 126
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11695905,
FT ECO:0007744|PDB:1I7P, ECO:0007744|PDB:1IB0"
FT BINDING 127
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11695905,
FT ECO:0007744|PDB:1I7P, ECO:0007744|PDB:1IB0"
FT BINDING 128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11695905,
FT ECO:0007744|PDB:1I7P, ECO:0007744|PDB:1IB0"
FT BINDING 185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11695905,
FT ECO:0007744|PDB:1I7P, ECO:0007744|PDB:1IB0"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00387"
FT MOD_RES 43
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00387"
FT MOD_RES 50
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN2"
FT MOD_RES 120
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN2"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:2498303,
FT ECO:0000269|PubMed:8978818"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1577871"
FT /id="VSP_009660"
FT VAR_SEQ 1..7
FT /note="MGAQLST -> MLGPLLWTASLPV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1577871"
FT /id="VSP_009661"
FT MUTAGEN 2
FT /note="G->A: Loss of myristoylation and localization to the
FT mitochondrial outer membrane but no loss of enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:8978818"
FT MUTAGEN 111
FT /note="K->E,Q: 2-3 fold decrease in Km for 2 Fe(III)-
FT [cytochrome b5]."
FT /evidence="ECO:0000269|PubMed:11695905"
FT MUTAGEN 111
FT /note="K->R,A,H: Km for 2 Fe(III)-[cytochrome b5] similiar
FT to that of wild-type."
FT /evidence="ECO:0000269|PubMed:11695905"
FT CONFLICT 33
FT /note="A -> M (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="F -> L (in Ref. 2; AAA41008)"
FT /evidence="ECO:0000305"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1I7P"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:1QX4"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1QX4"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 203..212
FT /evidence="ECO:0007829|PDB:1QX4"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1QX4"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:1QX4"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:1QX4"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:1QX4"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:1QX4"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:1QX4"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1QX4"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:1QX4"
SQ SEQUENCE 301 AA; 34175 MW; 45431A644413905F CRC64;
MGAQLSTLSR VVLSPVWFVY SLFMKLFQRS SPAITLENPD IKYPLRLIDK EIISHDTRRF
RFALPSPQHI LGLPIGQHIY LSTRIDGNLV IRPYTPVSSD DDKGFVDLVV KVYFKDTHPK
FPAGGKMSQY LENMNIGDTI EFRGPNGLLV YQGKGKFAIR ADKKSNPVVR TVKSVGMIAG
GTGITPMLQV IRAVLKDPND HTVCYLLFAN QSEKDILLRP ELEELRNEHS SRFKLWYTVD
KAPDAWDYSQ GFVNEEMIRD HLPPPGEETL ILMCGPPPMI QFACLPNLER VGHPKERCFT
F
//
